PPIL2_MOUSE
ID PPIL2_MOUSE Reviewed; 521 AA.
AC Q9D787; Q542A2; Q9CZL1;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=RING-type E3 ubiquitin-protein ligase PPIL2 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q13356};
DE AltName: Full=CYC4 {ECO:0000303|PubMed:15189447};
DE AltName: Full=Probable inactive peptidyl-prolyl cis-trans isomerase-like 2 {ECO:0000250|UniProtKB:Q13356};
DE Short=PPIase {ECO:0000250|UniProtKB:Q13356};
GN Name=Ppil2 {ECO:0000312|MGI:MGI:2447857};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP INTERACTION WITH CRNKL1 AND HSP90.
RX PubMed=15189447; DOI=10.1111/j.1356-9597.2004.00742.x;
RA Hatakeyama S., Matsumoto M., Yada M., Nakayama K.I.;
RT "Interaction of U-box-type ubiquitin-protein ligases (E3s) with molecular
RT chaperones.";
RL Genes Cells 9:533-548(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Has a ubiquitin-protein ligase activity acting as an E3
CC ubiquitin protein ligase or as an ubiquitin-ubiquitin ligase promoting
CC elongation of ubiquitin chains on substrates. By mediating 'Lys-48'-
CC linked polyubiquitination of proteins could target them for proteasomal
CC degradation. May also function as a chaperone, playing a role in
CC transport to the cell membrane of BSG/Basigin for instance. Probable
CC inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity.
CC {ECO:0000250|UniProtKB:Q13356}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q13356};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q13356}.
CC -!- SUBUNIT: Interacts with isoform 2 of BSG (By similarity). Interacts
CC (via the PPIase cyclophilin-type domain) with CRNKL1; they may form a
CC trimeric complex with HSP90. {ECO:0000250|UniProtKB:Q13356,
CC ECO:0000269|PubMed:15189447}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13356}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIL2
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: Despite the fact that it belongs to the cyclophilin-type
CC PPIase family, it has probably no peptidyl-prolyl cis-trans isomerase
CC activity due to the presence of a tyrosine instead of a tryptophan at
CC position 389. {ECO:0000250|UniProtKB:Q13356}.
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DR EMBL; AK009460; BAB26301.1; -; mRNA.
DR EMBL; AK090052; BAC41068.1; -; mRNA.
DR EMBL; AK161596; BAE36483.1; -; mRNA.
DR EMBL; BC028899; AAH28899.1; -; mRNA.
DR CCDS; CCDS27993.1; -.
DR RefSeq; NP_001239373.1; NM_001252444.1.
DR RefSeq; NP_001239374.1; NM_001252445.1.
DR RefSeq; NP_659203.1; NM_144954.3.
DR AlphaFoldDB; Q9D787; -.
DR SMR; Q9D787; -.
DR BioGRID; 211180; 2.
DR STRING; 10090.ENSMUSP00000023455; -.
DR iPTMnet; Q9D787; -.
DR PhosphoSitePlus; Q9D787; -.
DR EPD; Q9D787; -.
DR MaxQB; Q9D787; -.
DR PaxDb; Q9D787; -.
DR PeptideAtlas; Q9D787; -.
DR PRIDE; Q9D787; -.
DR ProteomicsDB; 289808; -.
DR Antibodypedia; 23562; 208 antibodies from 26 providers.
DR DNASU; 66053; -.
DR Ensembl; ENSMUST00000023455; ENSMUSP00000023455; ENSMUSG00000022771.
DR Ensembl; ENSMUST00000164458; ENSMUSP00000131422; ENSMUSG00000022771.
DR Ensembl; ENSMUST00000231712; ENSMUSP00000155861; ENSMUSG00000022771.
DR GeneID; 66053; -.
DR KEGG; mmu:66053; -.
DR UCSC; uc007yjx.2; mouse.
DR CTD; 23759; -.
DR MGI; MGI:2447857; Ppil2.
DR VEuPathDB; HostDB:ENSMUSG00000022771; -.
DR eggNOG; KOG0883; Eukaryota.
DR GeneTree; ENSGT00940000153189; -.
DR HOGENOM; CLU_012062_7_0_1; -.
DR InParanoid; Q9D787; -.
DR OMA; NFIKHCA; -.
DR OrthoDB; 1392223at2759; -.
DR PhylomeDB; Q9D787; -.
DR TreeFam; TF300854; -.
DR Reactome; R-MMU-210991; Basigin interactions.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 66053; 27 hits in 75 CRISPR screens.
DR ChiTaRS; Ppil2; mouse.
DR PRO; PR:Q9D787; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9D787; protein.
DR Bgee; ENSMUSG00000022771; Expressed in spermatocyte and 264 other tissues.
DR ExpressionAtlas; Q9D787; baseline and differential.
DR Genevisible; Q9D787; MM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; ISS:UniProtKB.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
DR CDD; cd16663; RING-Ubox_PPIL2; 1.
DR Gene3D; 2.40.100.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR044666; Cyclophilin_A-like.
DR InterPro; IPR026951; PPIL2_U-box_dom.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45625; PTHR45625; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF50891; SSF50891; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
DR PROSITE; PS51698; U_BOX; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Isopeptide bond; Nucleus; Reference proteome;
KW Transferase; Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..521
FT /note="RING-type E3 ubiquitin-protein ligase PPIL2"
FT /id="PRO_0000064172"
FT DOMAIN 35..108
FT /note="U-box"
FT DOMAIN 278..433
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT REGION 447..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 197..217
FT /evidence="ECO:0000255"
FT COMPBIAS 494..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 483
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q13356"
FT CROSSLNK 216
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13356"
FT CONFLICT 72
FT /note="K -> T (in Ref. 1; BAB26301)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 521 AA; 59065 MW; 9FFC202E7B4B9E7E CRC64;
MGKRQHQKDK MYITCAEYTH FYGGRKPDIS QTSFRRLPFD HCSLSLQPFV YPVCTPEGVV
FDLLNIVPWL KKYGTNPSTG EKLDGKSLIK LNFAKNSEGQ YHCPVLYSVF TDNTHIVAIR
TTGNVYTYEA VEQLNIKAKN LRDLLTDEPF SRQDIITLQD PTNLDKFNVS NFFHVKNNMR
IIDPDEEKAK QDPSYYLKNT NSETRETLQE LYKEFKGDEI LAATMRPPEK KKVDQLNAAH
YSTGKVSASF TSTAMVPETT HEAAVIDEDV LRYQFVKKKG YVRLHTNKGD LNLELHCDLT
PKTCENFIKL CKKQYYDGTI FHRSIRNFVI QGGDPTGTGT GGESFWGKPF KDEFRPNLSH
TGRGVLSMAN SGPNTNKSQF FITFRSCAYL DKKHTIFGRV VGGFDTLTAM ENVESDPKTD
RPKEEVLICT TTVFVDPYEE ADAQIAQERK KTQHQVDPEA KVKMSQPQPG NQGPQTYRQG
VGKYIHPAAT KRSAEEEPST STATPTAKKR PSRGFGDFSS W
